Search Results

Overview

Uniprot IDQ8TD19
Protein NameSerine/threonine-protein kinase Nek9
Gene NameNEK9
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
327 TLLNAPTKRPRSSTV
731 VEKVLNSKTIRSNSS

Function

Pleiotropic regulator of mitotic progression, participating in the control of spindle dynamics and chromosome separation (PubMed:12101123, PubMed:12840024, PubMed:14660563, PubMed:19941817). Phosphorylates different histones, myelin basic protein, beta-casein, and BICD2 (PubMed:11864968). Phosphorylates histone H3 on serine and threonine residues and beta-casein on serine residues (PubMed:11864968). Important for G1/S transition and S phase progression (PubMed:12840024, PubMed:14660563, PubMed:19941817). Phosphorylates NEK6 and NEK7 and stimulates their activity by releasing the autoinhibitory functions of Tyr-108 and Tyr-97 respectively (PubMed:12840024, PubMed:14660563, PubMed:19941817, PubMed:26522158)

Protein Sequence

10 MSVLGEYERH 20 CDSINSDFGS 30 ESGGCGDSSP 40 GPSASQGPRA 50 GGGAAEQEEL 60 HYIPIRVLGR 70 GAFGEATLYR 80 RTEDDSLVVW 90 KEVDLTRLSE 100 KERRDALNEI 110 VILALLQHDN 120 IIAYYNHFMD 130 NTTLLIELEY 140 CNGGNLYDKI 150 LRQKDKLFEE 160 EMVVWYLFQI 170 VSAVSCIHKA 180 GILHRDIKTL 190 NIFLTKANLI 200 KLGDYGLAKK 210 LNSEYSMAET 220 LVGTPYYMSP 230 ELCQGVKYNF 240 KSDIWAVGCV 250 IFELLTLKRT 260 FDATNPLNLC 270 VKIVQGIRAM 280 EVDSSQYSLE 290 LIQMVHSCLD 300 QDPEQRPTAD 310 ELLDRPLLRK 320 RRREMEEKVT 330 LLNAPTKRPR 340 SSTVTEAPIA 350 VVTSRTSEVY 360 VWGGGKSTPQ 370 KLDVIKSGCS 380 ARQVCAGNTH 390 FAVVTVEKEL 400 YTWVNMQGGT 410 KLHGQLGHGD 420 KASYRQPKHV 430 EKLQGKAIRQ 440 VSCGDDFTVC 450 VTDEGQLYAF 460 GSDYYGCMGV 470 DKVAGPEVLE 480 PMQLNFFLSN 490 PVEQVSCGDN 500 HVVVLTRNKE 510 VYSWGCGEYG 520 RLGLDSEEDY 530 YTPQKVDVPK 540 ALIIVAVQCG 550 CDGTFLLTQS 560 GKVLACGLNE 570 FNKLGLNQCM 580 SGIINHEAYH 590 EVPYTTSFTL 600 AKQLSFYKIR 610 TIAPGKTHTA 620 AIDERGRLLT 630 FGCNKCGQLG 640 VGNYKKRLGI 650 NLLGGPLGGK 660 QVIRVSCGDE 670 FTIAATDDNH 680 IFAWGNGGNG 690 RLAMTPTERP 700 HGSDICTSWP 710 RPIFGSLHHV 720 PDLSCRGWHT 730 ILIVEKVLNS 740 KTIRSNSSGL 750 SIGTVFQSSS 760 PGGGGGGGGG 770 EEEDSQQESE 780 TPDPSGGFRG 790 TMEADRGMEG 800 LISPTEAMGN 810 SNGASSSCPG 820 WLRKELENAE 830 FIPMPDSPSP 840 LSAAFSESEK 850 DTLPYEELQG 860 LKVASEAPLE 870 HKPQVEASSP 880 RLNPAVTCAG 890 KGTPLTPPAC 900 ACSSLQVEVE 910 RLQGLVLKCL 920 AEQQKLQQEN 930 LQIFTQLQKL 940 NKKLEGGQQV 950 GMHSKGTQTA 960 KEEMEMDPKP 970 DLDSDSWCLL GTDSCRPSL

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005634 nucleus
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0046872 metal ion binding
Molecular Function GO:0030295 protein kinase activator activity
Molecular Function GO:0019901 protein kinase binding
Molecular Function GO:0106310 protein serine kinase activity
Molecular Function GO:0004674 protein serine/threonine kinase activity
Biological Process GO:0051301 cell division
Biological Process GO:0000278 mitotic cell cycle
Biological Process GO:0007346 regulation of mitotic cell cycle

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.